The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Clustering of Fluorine-Substituted Alcohols as a Factor Responsible for Their Marked Effects on Proteins and Peptides
Abstract
Among various alcohols, those substituted with fluorine, such as 2,2,2-trifluoroethanol (TFE) or 3,3,3,3‘,3‘,3‘-hexafluoro-2-propanol (HFIP), have a marked potential to induce the formation of α-helical structures in peptides and to denature the native structures of proteins. However, the mechanism by which these alcohols exert their effects is unknown. Melittin, a bee venom peptide, is unfolded in the absence of alcohol, but is transformed to an α-helical structure upon addition of alcohols. On the other hand, addition of alcohols to β-lactoglobulin, a predominantly β-sheet protein, denatures the molecule and transforms it to an α-helical structure. We examined the role of several factors in these alcohol-induced transitions, i.e., relative dielectric constant, strength of hydrogen bond estimated by the pH titration of salicylic acid, and clustering of alcohol molecules measured by solution X-ray scattering. Although relative dielectric constant and hydrogen bond strength were confirmed to be important, they did not explain the marked effects of TFE and HFIP. X-ray scattering detected clusters of TFE or HFIP molecules in alcohol/water mixtures with a maximum at around 30% (v/v) of each alcohol. When the conformational transitions induced by TFE and HFIP were plotted against the extent of cluster formation by the corresponding alcohol/water mixtures, the TFE and HFIP-induced transition curves agreed with each other for both melittin and β-lactoglobulin. This suggests that clustering of alcohol molecules is an important factor that enhances the effects of alcohols on proteins and peptides.
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Citations
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Cited by
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Metadata
- Authors
- Hong, D.-P., Hoshino, M., Kuboi, R., & Goto, Y.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-08-05
- Volume
- 121
- Issue
- 37
- Pages
- 8427-8433
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2006570293
- Cited by
- 377
- References
- 21
- FWCI
- 1.85
- Type
- journal article
- Language
- en
- Open access
- closed
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